InChI key
AQGZJQNZNONGKY-UHFFFAOYSA-N
InChI
1S/C14H8N2O4/c17-11-5-6-12(18)15(11)9-1-2-10(4-3-9)16-13(19)7-8-14(16)20/h1-8H
SMILES string
O=C1C=CC(=O)N1c2ccc(cc2)N3C(=O)C=CC3=O
assay
97%
form
powder
mp
>300 °C (lit.)
E Pate et al.
Biochemistry, 36(40), 12155-12166 (1997-10-07)
A series of ATP analogs, in which moieties of various sizes have been added to the gamma-phosphorus of ATP, bind to the active site of myosin and to the actomyosin complex in myofibrils and in chemically skinned fibers. The affinity
Yoshitaka Kimori et al.
The Biochemical journal, 450(1), 23-35 (2012-12-06)
In the present paper, we described our attempt to characterize the rough three-dimensional features of the structural analogue of the key intermediate of myosin's cross-bridge cycle. Using quick-freeze deep-etch replica electron microscopy, we observed that actin-attached myosin during in vitro
Agnieszka Galińska-Rakoczy et al.
Journal of molecular biology, 387(4), 869-882 (2009-04-03)
The mechanism of salt-induced actin polymerization involves the energetically unfavorable nucleation step, followed by filament elongation by the addition of monomers. The use of a bifunctional cross-linker, N,N'-(1,4-phenylene)dimaleimide, revealed rapid formation of the so-called lower dimers (LD) in which actin
Yu S Borovikov et al.
Biophysical journal, 86(5), 3020-3029 (2004-04-28)
Fluorescence polarization measurements were used to study changes in the orientation and order of different sites on actin monomers within muscle thin filaments during weak or strong binding states with myosin subfragment-1. Ghost muscle fibers were supplemented with actin monomers
L K Nitao et al.
Biochemistry, 37(47), 16704-16710 (1998-12-08)
Previous biochemical studies have shown that the SH1 (Cys707) and SH2 (Cys697) groups on rabbit skeletal myosin subfragment 1 (S1) can be cross-linked by using reagents of different cross-linking lengths. In the presence of nucleotide, this cross-linking is accelerated. In
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